Entry Database : PDB / ID : 2b07 Structure visualization Downloads & linksTitle Crystal structure of PTP1B with Tricyclic Thiophene inhibitor. ComponentsTyrosine-protein phosphatase, non-receptor type 1 Details Keywords HYDROLASE / PROTEIN TYROSINE PHOSPHATASE / Hydrolyase / tricyclic ThiophenesFunction / homology Function and homology informationFunction Domain/homology Component
regulation of hepatocyte growth factor receptor signaling pathway / PTK6 Down-Regulation / positive regulation of receptor catabolic process / insulin receptor recycling / peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity / negative regulation of vascular endothelial growth factor receptor signaling pathway / negative regulation of PERK-mediated unfolded protein response / regulation of intracellular protein transport / IRE1-mediated unfolded protein response / cytoplasmic side of endoplasmic reticulum membrane ... regulation of hepatocyte growth factor receptor signaling pathway / PTK6 Down-Regulation / positive regulation of receptor catabolic process / insulin receptor recycling / peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity / negative regulation of vascular endothelial growth factor receptor signaling pathway / negative regulation of PERK-mediated unfolded protein response / regulation of intracellular protein transport / IRE1-mediated unfolded protein response / cytoplasmic side of endoplasmic reticulum membrane / platelet-derived growth factor receptor-beta signaling pathway / sorting endosome / mitochondrial crista / positive regulation of IRE1-mediated unfolded protein response / regulation of type I interferon-mediated signaling pathway / regulation of endocytosis / non-membrane spanning protein tyrosine phosphatase activity / positive regulation of protein tyrosine kinase activity / peptidyl-tyrosine dephosphorylation / Regulation of IFNA/IFNB signaling / regulation of signal transduction / cellular response to unfolded protein / growth hormone receptor signaling pathway via JAK-STAT / negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / negative regulation of signal transduction / Regulation of IFNG signaling / MECP2 regulates neuronal receptors and channels / Growth hormone receptor signaling / endoplasmic reticulum unfolded protein response / positive regulation of JUN kinase activity / negative regulation of insulin receptor signaling pathway / Insulin receptor recycling / ephrin receptor binding / Integrin signaling / protein dephosphorylation / protein-tyrosine-phosphatase / negative regulation of MAP kinase activity / protein phosphatase 2A binding / protein tyrosine phosphatase activity / endosome lumen / insulin receptor binding / Negative regulation of MET activity / negative regulation of ERK1 and ERK2 cascade / receptor tyrosine kinase binding / insulin receptor signaling pathway / actin cytoskeleton organization / early endosome / mitochondrial matrix / cadherin binding / protein kinase binding / enzyme binding / endoplasmic reticulum / protein-containing complex / RNA binding / zinc ion binding / cytosol / cytoplasm Similarity search - Function Protein-tyrosine phosphatase, non-receptor type-1/2 / : / Protein tyrosine phosphatase superfamily / Protein-Tyrosine Phosphatase; Chain A / Protein tyrosine phosphatase, catalytic domain / PTP type protein phosphatase domain profile. / Protein-tyrosine phosphatase / Tyrosine-specific protein phosphatase, PTPase domain / Protein-tyrosine phosphatase, catalytic / Protein tyrosine phosphatase, catalytic domain motif ... Protein-tyrosine phosphatase, non-receptor type-1/2 / : / Protein tyrosine phosphatase superfamily / Protein-Tyrosine Phosphatase; Chain A / Protein tyrosine phosphatase, catalytic domain / PTP type protein phosphatase domain profile. / Protein-tyrosine phosphatase / Tyrosine-specific protein phosphatase, PTPase domain / Protein-tyrosine phosphatase, catalytic / Protein tyrosine phosphatase, catalytic domain motif / Tyrosine specific protein phosphatases active site. / Protein-tyrosine phosphatase, active site / Tyrosine-specific protein phosphatases domain / Tyrosine specific protein phosphatases domain profile. / Protein-tyrosine phosphatase-like / Alpha-Beta Complex / Alpha Beta Similarity search - Domain/homologyBiological species Homo sapiens (human)Method X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution : 2.1 Å DetailsAuthors Moretto, A.F. / Kirincich, S.J. / Xu, W.X. / Smith, M.J. / Wan, Z.K. / Wilson, D.P. / Follows, B.C. / Binnun, E. / Joseph-McCarthy, D. / Foreman, K. ...Moretto, A.F. / Kirincich, S.J. / Xu, W.X. / Smith, M.J. / Wan, Z.K. / Wilson, D.P. / Follows, B.C. / Binnun, E. / Joseph-McCarthy, D. / Foreman, K. / Erbe, D.V. / Zhang, Y.L. / Tam, S.K. / Tam, S.Y. / Lee, J. CitationJournal : Bioorg.Med.Chem. / Year : 2006Title : Bicyclic and tricyclic thiophenes as protein tyrosine phosphatase 1B inhibitors.Authors : Moretto, A.F. / Kirincich, S.J. / Xu, W.X. / Smith, M.J. / Wan, Z.K. / Wilson, D.P. / Follows, B.C. / Binnun, E. / Joseph-McCarthy, D. / Foreman, K. / Erbe, D.V. / Zhang, Y.L. / Tam, S.K. / Tam, S.Y. / Lee, J. History Deposition Sep 13, 2005 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Dec 6, 2005 Provider : repository / Type : Initial releaseRevision 1.1 May 1, 2008 Group : Version format complianceRevision 1.2 Jul 13, 2011 Group : Version format complianceRevision 1.3 Feb 14, 2024 Group : Data collection / Database references / Derived calculationsCategory : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / struct_site Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Show all Show less Remark 42 MOLPROBITY STRUCTURE VALIDATION PROGRAMS : MOLPROBITY (KING, REDUCE, AND PROBE) AUTHORS : I.W. ... MOLPROBITY STRUCTURE VALIDATION PROGRAMS : MOLPROBITY (KING, REDUCE, AND PROBE) AUTHORS : I.W.DAVIS,J.M.WORD URL : HTTP://KINEMAGE.BIOCHEM.DUKE.EDU/MOLPROBITY/ AUTHORS : J.S.RICHARDSON,W.B.ARENDALL,D.C.RICHARDSON REFERENCE : NEW TOOLS AND DATA FOR IMPROVING : STRUCTURES, USING ALL-ATOM CONTACTS : METHODS IN ENZYMOLOGY. 2003;374:385-412. MOLPROBITY OUTPUT SCORES: ALL-ATOM CLASHSCORE : 5.78 (0.00 B<40) BAD ROTAMERS : 0.0% 0/270 (TARGET 0-1%) RAMACHANDRAN OUTLIERS : 0.3% 1/295 (TARGET 0.2%) RAMACHANDRAN FAVORED : 97.6% 288/295 (TARGET 98.0%)